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Last update 08 May 2025

MBL x MBL superfamily

Last update 08 May 2025

Basic Info

Related Targets

MBLMBL superfamily

Drugs associated with MBL x MBL superfamily

US20240335453

Patent Mining

Target

MBL x MBL superfamily

Mechanism

MBL inhibitors

Active Org.

University of KwaZulu-Natal [+1]

Originator Org.

University of Zululand [+1]

Active Indication

Bacterial Infections

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with MBL x MBL superfamily

100 Translational Medicine associated with MBL x MBL superfamily

0 Patents (Medical) associated with MBL x MBL superfamily

258

Literatures (Medical) associated with MBL x MBL superfamily

01 Apr 2025·Mymensingh medical journal : MMJ

The Pool of Beta-lactamase Present in Extended Drug Resistant Klebsiella pneumoniae Isolated from Clinical Settings in Dhaka, Bangladesh.

Article

Author: Islam, M F ; Khaleque, M ; Akter, S ; Begum, A ; Akhter, H ; Tabassum, T

Recently bacterial infections caused by antibiotic resistant bacteria are becoming a threat to the health care system of many countries. Extensively-drug-resistant (XDR) Klebsiella pneumoniae are resistant to almost all classes of antibiotics and only a few are for clinical use. Recent emergence, worldwide dissemination and clinical impact of carbapenemase positive isolates persuade us to characterize the clinical K. pneumoniae isolates. We tested 647 K. pneumoniae that was isolated from different specimens of hospitalized patients in Dhaka, Bangladesh. Various phenotypic characterization, plasmid profiling and PCR assays followed by sequencing were performed. Round the year, 4.33% (n=28) K. pneumoniae isolates were found as XDR in addition to carbapenem resistant. Among the XDR isolates, 82.0% (n=23) showed Metallo-beta-lactamase (MBL) phenotype. Only two isolates showed MBL with KPC (K. pneumoniae carbapenemase) phenotype. By double disc synergy test, 12 isolates (43.0%) showed extended-spectrum beta-lactamase (ESBL) phenotype in addition. Among the isolates, 60.0% (n=17) were blaTEM positive, 82.0% (n=23) were blaSHV positive and 46.0% (n=13) were blaOXA positive determined by multiplex PCR. BlaCTX-M were present in 43.0% (n=12) isolates, which were of type-15 as revealed by sequencing. More than 60.0% (n=17) isolates were positive for blaNDM-1. Multiple genes coexisted in nearly all isolates. None of those were found to carry blaVIM or blaKPC. Twenty-six isolates were found to be strong biofilm former. Among the isolates, 16 harbored multiple plasmids ranging from 19 to 91 KDa; however, correlation between plasmid profile and antibiotic resistance pattern was not evident. Prevalence of carbapenem resistant and ESBL isolates have been previously reported in Bangladesh. Therefore, this study will expand our knowledge about XDR disseminated in Bangladesh and could assist in future therapeutic management.

01 Apr 2025·Journal of Infection and Chemotherapy

An evaluation of the modified carbapenem inactivation method (mCIM) in conjunction with EDTA or sodium mercaptoacetate, for detecting metallo β-lactamase production for Aeromonas species harboring blaCphA

Article

Author: Nakano, Ami ; Nishiyama, Naoya ; Uechi, Kohei ; Yamamoto, Kazuko ; Nakamura, Tatsuya ; Arakaki, Wakako ; Maeda, Shiro ; Uechi, Ayumi

Several Aeromonas species, including Aeromonas hydrophila, have been known to produce CphA, a chromosomal metallo β-lactamase (MBL). We aimed to evaluate the clinical usefulness of modified carbapenem inactivation method (mCIM) in conjunction with EDTA (eCIM) or sodium mercaptoacetate (SMA-mCIM) for MBL-producing Aeromonas species. Fifty-six clinical isolates of Aeromonas species stored at the University of the Ryukyus Hospital were used in this study. The antimicrobial susceptibility testing was performed using a VITEK®2 AST-N404 card (bioMerieux, Marcy-l'Etoile, France) and the results were interpreted according to the CLSI guideline M45 3rd edition. The carbapenemase genes, namely bla_GES, bla_IMP, bla_KPC, bla_NDM, bla_OXA-48-like, bla_VIM, and bla_CphA, were detected by PCR. The production of carbapenemase was evaluated using the mCIM and the differentiation of MBL was eCIM and SMA-mCIM. The resistance rates to imipenem and meropenem were 21.4 % (12/56) and 32.1 % (18/56), respectively. The mCIM showed a sensitivity of 100 % (33/33 bla_CphA positive isolates) and a specificity of 95.7 % (22/23 bla_CphA negative isolates) for the tested isolates. Among the 33 mCIM-positive isolates, 29 (87.9 %) for eCIM, and 6 (18.2 %) for SMA-mCIM were judged as MBL positive, respectively. It is suggested that the mCIM in conjunction with EDTA is useful for detecting MBL production in Aeromonas species harboring bla_CphA.

14 Mar 2025·ACS Infectious Diseases

AHM-1: An Inclusion to the Arsenal of β-Lactam Resistance in Clostridioides difficile

Article

Author: Mukherjee, Abirlal ; Roy, Partha ; Basu, Sulagna ; Hazra, Saugata ; Dhankhar, Kunal ; Ghosh, Chandrachur ; Adhikary, Rajsekhar ; Barman, Jyoti

This study delves into a newly discovered MBL (metallo-β-lactamase) in Clostridioides difficile, a formidable pathogen known for causing nosocomial infections and exhibiting resistance to antimicrobial agents. The primary objective was to unravel its structure-function relationship. This research establishes the enzyme AHM-1 as a subclass B3-like MBL. Experimental results reveal that the enzyme's active site consists of two Zn²⁺ atoms exhibiting tetrahedral and trigonal bipyramidal coordination, similar to B1 and B3 MBLs. Notably, within its active site, it exhibits a lower binding capacity for other transition metal ions such as Fe²⁺, Mn²⁺, and Ni²⁺ compared to Zn²⁺. The zinc-binding sites of B1 and B3 MBLs contain strictly conserved His116-His118-His196 and Asp120-Cys221/His121-His263. The absence of all the conserved residues except His116, Asp120, and His121 in the Zn-binding site distinctly separates this enzyme from these two MBL subclasses. Conserved zinc binding motifs present in B1 and B3 MBLs are H-X-H-X-D and H-X-H-X-D-H, respectively. The presence of the H-X-D-X-D-H motif in the enzyme, similar to that in B3 enzymes, along with sequence and structural analysis, places this new enzyme closer to the enzymes belonging to the B3 subclass. This study also identifies the likely catalytic residues responsible for its β-lactamase activity, similar to B3 MBLs. In contrast to MBLs, this enzyme displays hydrolytic activity toward aztreonam. It also shows higher catalytic efficiency toward higher generation cephalosporins. This study thus underscores the significance of a novel enzyme with β-lactamase activity in Clostridioides difficile, highlighting its potential implications for clinical treatment due to its disparities from conventional MBLs.

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